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Database: UniProt
Entry: N1PPU7_DOTSN
LinkDB: N1PPU7_DOTSN
Original site: N1PPU7_DOTSN 
ID   N1PPU7_DOTSN            Unreviewed;       423 AA.
AC   N1PPU7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Choline monooxygenase, chloroplastic {ECO:0000256|ARBA:ARBA00014931};
DE            EC=1.14.15.7 {ECO:0000256|ARBA:ARBA00012763};
GN   ORFNames=DOTSEDRAFT_53545 {ECO:0000313|EMBL:EME44449.1};
OS   Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight
OS   fungus) (Mycosphaerella pini).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX   NCBI_TaxID=675120 {ECO:0000313|EMBL:EME44449.1, ECO:0000313|Proteomes:UP000016933};
RN   [1] {ECO:0000313|Proteomes:UP000016933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX   PubMed=23209441; DOI=10.1371/journal.pgen.1003088;
RA   de Wit P.J.G.M., van der Burgt A., Oekmen B., Stergiopoulos I.,
RA   Abd-Elsalam K.A., Aerts A.L., Bahkali A.H., Beenen H.G., Chettri P.,
RA   Cox M.P., Datema E., de Vries R.P., Dhillon B., Ganley A.R.,
RA   Griffiths S.A., Guo Y., Hamelin R.C., Henrissat B., Kabir M.S.,
RA   Jashni M.K., Kema G., Klaubauf S., Lapidus A., Levasseur A., Lindquist E.,
RA   Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A., Schijlen E.,
RA   Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S., Goodwin S.B.,
RA   Grigoriev I.V., Collemare J., Bradshaw R.E.;
RT   "The genomes of the fungal plant pathogens Cladosporium fulvum and
RT   Dothistroma septosporum reveal adaptation to different hosts and lifestyles
RT   but also signatures of common ancestry.";
RL   PLoS Genet. 8:E1003088-E1003088(2012).
RN   [2] {ECO:0000313|EMBL:EME44449.1, ECO:0000313|Proteomes:UP000016933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
CC   -!- FUNCTION: Catalyzes the first step of the osmoprotectant glycine
CC       betaine synthesis. {ECO:0000256|ARBA:ARBA00002149}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=choline + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] =
CC         betaine aldehyde hydrate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin];
CC         Xref=Rhea:RHEA:17769, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC         ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:15870, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738; EC=1.14.15.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00001883};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC       choline pathway; betaine aldehyde from choline (monooxygenase route):
CC       step 1/1. {ECO:0000256|ARBA:ARBA00004866}.
CC   -!- SIMILARITY: Belongs to the choline monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00010848}.
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DR   EMBL; KB446539; EME44449.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1PPU7; -.
DR   STRING; 675120.N1PPU7; -.
DR   EnsemblFungi; EME44449; EME44449; DOTSEDRAFT_53545.
DR   eggNOG; ENOG502QQJW; Eukaryota.
DR   HOGENOM; CLU_026244_1_2_1; -.
DR   OMA; YAFILVK; -.
DR   OrthoDB; 297304at2759; -.
DR   UniPathway; UPA00529; UER00430.
DR   Proteomes; UP000016933; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0019133; F:choline monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
DR   CDD; cd00680; RHO_alpha_C; 1.
DR   CDD; cd03469; Rieske_RO_Alpha_N; 1.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR   InterPro; IPR001663; Rng_hydr_dOase-A.
DR   PANTHER; PTHR43756; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43756:SF5; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   Pfam; PF00848; Ring_hydroxyl_A; 1.
DR   PRINTS; PR00090; RNGDIOXGNASE.
DR   SUPFAM; SSF55961; Bet v1-like; 1.
DR   SUPFAM; SSF50022; ISP domain; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016933}.
FT   DOMAIN          59..146
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   423 AA;  49091 MW;  569DAD90FA6C74BF CRC64;
     MPSKRQDSIT DTVFNWLGYG GSVSEAKEEK QAMRALPANW YQSEEMYQLE RRSIFSRKWQ
     LISHKCRLPK PGDWLKFEIA NFSFVITHDR TGQFNAFHNV CRHRAFPVVT EGSGTSRIFS
     CKYHGWSYGL NGKLAKAPGY QELEGFDKEK NSLMPIHLHV DRNGFMYVNL DAKETPEIAW
     EDDMIGMDTQ ERYRDFNFAD YEFDHFWEME GDYNWKILAD NYNECYHCAT SHPDIGAVAN
     LQSYSVDTAR GQIVHNPATT QEQRDAGLVV ASTYYFPNVS TNITPHFFMI QRFVPSSPSK
     SSMQYQVFRN KNSTDEQFDL VNQIYKRVMS EDKYLCNLAQ KNINAGIFTN GELHPRLEKG
     PLYFQSNVRD NVMEHFEKEK RARKEIWPAR PELPQTGSTS VSKKDMEFCS GLSCATTPKE
     LTW
//
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